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Search results 601 to 700 out of 907 for Traf6

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Type Details Score
Publication
30692626 | J:282869
First Author: Wang G
Year: 2019
Journal: Nat Cell Biol
Title: SETDB1-mediated methylation of Akt promotes its K63-linked ubiquitination and activation leading to tumorigenesis.
Volume: 21
Issue: 2
Pages: 214-225
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Publication
29228365 | J:281773
First Author: Zheng R
Year: 2018
Journal: J Infect Dis
Title: Notch4 Negatively Regulates the Inflammatory Response to Mycobacterium tuberculosis Infection by Inhibiting TAK1 Activation.
Volume: 218
Issue: 2
Pages: 312-323
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Publication
23042150 | J:188557
First Author: Zhong B
Year: 2012
Journal: Nat Immunol
Title: Negative regulation of IL-17-mediated signaling and inflammation by the ubiquitin-specific protease USP25.
Volume: 13
Issue: 11
Pages: 1110-7
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Publication
22632973 | J:186169
First Author: Chan CH
Year: 2012
Journal: Cell
Title: The Skp2-SCF E3 ligase regulates Akt ubiquitination, glycolysis, herceptin sensitivity, and tumorigenesis.
Volume: 149
Issue: 5
Pages: 1098-111
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Publication
32732870 | J:295201
First Author: Balic JJ
Year: 2020
Journal: Nat Commun
Title: STAT3 serine phosphorylation is required for TLR4 metabolic reprogramming and IL-1β expression.
Volume: 11
Issue: 1
Pages: 3816
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Publication
30996248 | J:275578
First Author: Ben J
Year: 2019
Journal: Nat Commun
Title: Major vault protein suppresses obesity and atherosclerosis through inhibiting IKK-NF-κB signaling mediated inflammation.
Volume: 10
Issue: 1
Pages: 1801
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Publication
24316060 | J:207916
 
First Author: Wang L
Year: 2014
Journal: Neuroscience
Title: The role of miR-146a in dorsal root ganglia neurons of experimental diabetic peripheral neuropathy.
Volume: 259
Pages: 155-63
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Publication
29867947 | J:284732
 
First Author: Yao Y
Year: 2018
Journal: Front Immunol
Title: Tespa1 Deficiency Dampens Thymus-Dependent B-Cell Activation and Attenuates Collagen-Induced Arthritis in Mice.
Volume: 9
Pages: 965
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Publication
28846086 | J:271836
First Author: Zheng Q
Year: 2017
Journal: Nat Immunol
Title: The RNA helicase DDX46 inhibits innate immunity by entrapping m6A-demethylated antiviral transcripts in the nucleus.
Volume: 18
Issue: 10
Pages: 1094-1103
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Publication
29734366 | J:324167
First Author: Zhang L
Year: 2018
Journal: PLoS Pathog
Title: Induction of OTUD1 by RNA viruses potently inhibits innate immune responses by promoting degradation of the MAVS/TRAF3/TRAF6 signalosome.
Volume: 14
Issue: 5
Pages: e1007067
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Publication
18347055 | J:136090
First Author: Conze DB
Year: 2008
Journal: Mol Cell Biol
Title: Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-kappaB activation.
Volume: 28
Issue: 10
Pages: 3538-47
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Publication
32035036 | J:287739
First Author: Wu Y
Year: 2020
Journal: Mol Cell
Title: Dopamine Uses the DRD5-ARRB2-PP2A Signaling Axis to Block the TRAF6-Mediated NF-κB Pathway and Suppress Systemic Inflammation.
Volume: 78
Issue: 1
Pages: 42-56.e6
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Publication
33159854 | J:305825
First Author: Lefkopoulos S
Year: 2020
Journal: Immunity
Title: Repetitive Elements Trigger RIG-I-like Receptor Signaling that Regulates the Emergence of Hematopoietic Stem and Progenitor Cells.
Volume: 53
Issue: 5
Pages: 934-951.e9
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Publication
37657242 | J:340601
First Author: Liu B
Year: 2023
Journal: Int Immunopharmacol
Title: USP25 ameliorates diabetic nephropathy by inhibiting TRAF6-mediated inflammatory responses.
Volume: 124
Issue: Pt A
Pages: 110877
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Protein
Q8C245
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: false
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Protein Domain
IPR012227 | TNF_rcpt-assoc_TRAF_met
Type: Family
Description: The tumour necrosis factor (TNF) receptor associated factors (TRAFs) are major signal transducers for the TNF receptor (TNFR) superfamily and the interleukin-1 receptor/Toll-like receptor superfamily in mammals []. TRAFs constitute a family of genetically conserved adapter proteins found in mammals (TRAF1-6) as well as in other multicellular organisms such as Drosophila [], Caenorhabditis elegans []. TRAF2 is the prototypical member of the family. Mammalian TRAF1 and TRAF2 were the first members initially identified by their association with TNFR2. The TRAF1/TRAF2 and TRAF3/TRAF5 gene pairs may have arisen from recent independent gene duplications and to share a common ancestral gene. TRAF4 and TRAF6 precursor genes may have arisen earlier during evolution, with the divergence of the TRAF6 precursor occurring earliest of all. Except TRAF1, this PIRSF has a general domain architecture containing one N-terminal RING finger, a variable number of middle region of TRAF-type zinc finger and C2H2 type of zinc finger, and one C-terminal MATH domain. TRAF1 is unique in the family in that it lacks the N-terminal RING and zinc-finger domains []. This has rendered TRAF1 unable to promote TNF receptor signalling and act as a "dominant negative"TRAF []. Also TRAF1 is a substrate for caspases activated by TNF family death receptors []. The larger C-terminal cleaved fragment can bind to and sequester TRAF2 from TNFR1 complex, therefore modulating TNF induced NFkB activation []. A wide range of biological functions, such as adaptive and innate immunity, embryonic development, stress response and bone metabolism, are mediated by TRAFs through the induction of cell survival, proliferation, differentiation and death. TRAFs are functionally divergent from a perspective of both upstream and downstream TRAF signal transduction pathways and of signalling-dependent regulation of TRAF trafficking. Each TRAF protein interacts with and mediates the signal transduction of multiple receptors, and in turn each receptor utilises multiple TRAFs for specific functions []. About 40 interaction partners of TRAF have been described thus far, including receptors, kinases, regulators and adaptor proteins.TRAF proteins can be recruited to and activated by ligand-engaged receptors in least three distinct ways []. 1) Members of the TNFR superfamily that do not contain intracellular death domains, such as TNFR2 and CD40, recruit TRAFs directly via short sequences in their intracellular tails []. 2) Those that contain an intracellular death domain, such as TNFR1, first recruit an adapter protein, TRADD, via a death-domain-death-domain interaction, which then serves as a central platform of the TNFR1 signalling complex, which assembles TRAF2 and RIP for survival signalling, and FADD and caspase-8 for the induction of apoptosis. 3) Members of the IL-1R/TLR superfamily contain a protein interaction module known as the TIR domain, which recruits, sequentially, MyD88, a TIR domain and death domain containing protein, and IRAKs, adapter Ser/Thr kinases with death domains. IRAKs in turn associate with TRAF6 to elicit signalling by IL-1 and pathogenic components such as LPS. A common mechanism for the membrane-proximal event in TRAF signalling has been revealed by the conserved trimeric association in the crystal structure of the TRAF domain of TRAF2 [].This entry represents the TNF receptor associated factors found in metazoa.
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Protein Domain
IPR043211 | TNF_rcpt-assoc_TRAF
Type: Family
Description: The tumour necrosis factor (TNF) receptor associated factors (TRAFs) are major signal transducers for the TNF receptor (TNFR) superfamily and the interleukin-1 receptor/Toll-like receptor superfamily in mammals []. TRAFs constitute a family of genetically conserved adapter proteinsfound in mammals (TRAF1-6) as well as in other multicellular organisms such as Drosophila [], Caenorhabditis elegans []. TRAF2 is the prototypical member of the family. Mammalian TRAF1 and TRAF2 were the first members initially identified by their association with TNFR2. The TRAF1/TRAF2 and TRAF3/TRAF5 gene pairs may have arisen from recent independent gene duplications and to share a common ancestral gene. TRAF4 and TRAF6 precursor genes may have arisen earlier during evolution, with the divergence of the TRAF6 precursor occurring earliest of all. Except TRAF1, this PIRSF has a general domain architecture containing one N-terminal RING finger, a variable number of middle region of TRAF-type zinc finger and C2H2 type of zinc finger, and one C-terminal MATH domain. TRAF1 is unique in the family in that it lacks the N-terminal RING and zinc-finger domains []. This has rendered TRAF1 unable to promote TNF receptor signalling and act as a "dominant negative"TRAF []. Also TRAF1 is a substrate for caspases activated by TNF family death receptors []. The larger C-terminal cleaved fragment can bind to and sequester TRAF2 from TNFR1 complex, therefore modulating TNF induced NFkB activation []. A wide range of biological functions, such as adaptive and innate immunity, embryonic development, stress response and bone metabolism, are mediated by TRAFs through the induction of cell survival, proliferation, differentiation and death. TRAFs are functionally divergent from a perspective of both upstream and downstream TRAF signal transduction pathways and of signalling-dependent regulation of TRAF trafficking. Each TRAF protein interacts with and mediates the signal transduction of multiple receptors, and in turn each receptor utilises multiple TRAFs for specific functions []. About 40 interaction partners of TRAF have been described thus far, including receptors, kinases, regulators and adaptor proteins.TRAF proteins can be recruited to and activated by ligand-engaged receptors in least three distinct ways []. 1) Members of the TNFR superfamily that do not contain intracellular death domains, such as TNFR2 and CD40, recruit TRAFs directly via short sequences in their intracellular tails []. 2) Those that contain an intracellular death domain, such as TNFR1, first recruit an adapter protein, TRADD, via a death-domain-death-domain interaction, which then serves as a central platform of the TNFR1 signalling complex, which assembles TRAF2 and RIP for survival signalling, and FADD and caspase-8 for the induction of apoptosis. 3) Members of the IL-1R/TLR superfamily contain a protein interaction module known as the TIR domain, which recruits, sequentially, MyD88, a TIR domain and death domain containing protein, and IRAKs, adapter Ser/Thr kinases with death domains. IRAKs in turn associate with TRAF6 to elicit signalling by IL-1 and pathogenic components such as LPS. A common mechanism for the membrane-proximal event in TRAF signalling has been revealed by the conserved trimeric association in the crystal structure of the TRAF domain of TRAF2 [].
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Publication
8069916 | J:19898
First Author: Rothe M
Year: 1994
Journal: Cell
Title: A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.
Volume: 78
Issue: 4
Pages: 681-92
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Publication
11865024 | -
First Author: Chung JY
Year: 2002
Journal: J Cell Sci
Title: All TRAFs are not created equal: common and distinct molecular mechanisms of TRAF-mediated signal transduction.
Volume: 115
Issue: Pt 4
Pages: 679-88
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Publication
22539786 | J:188742
First Author: Zhao W
Year: 2012
Journal: J Immunol
Title: Tripartite motif-containing protein 38 negatively regulates TLR3/4- and RIG-I-mediated IFN-β production and antiviral response by targeting NAP1.
Volume: 188
Issue: 11
Pages: 5311-8
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Protein
Q3TB04
Organism: Mus musculus/domesticus
Length: 737  
Fragment?: false
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Protein
Q6PE61
Organism: Mus musculus/domesticus
Length: 687  
Fragment?: false
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Protein
H3BJN6
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
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Protein
Q8C0E8
Organism: Mus musculus/domesticus
Length: 687  
Fragment?: false
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Protein
Q8K0I1
Organism: Mus musculus/domesticus
Length: 549  
Fragment?: true
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Publication
19913487 | -
First Author: Oda S
Year: 2009
Journal: Structure
Title: Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7.
Volume: 17
Issue: 11
Pages: 1528-37
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Publication
30355448 | -
   
First Author: Luong P
Year: 2018
Journal: Elife
Title: INAVA-ARNO complexes bridge mucosal barrier function with inflammatory signaling.
Volume: 7
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Publication
27044754 | J:281253
First Author: Yan X
Year: 2016
Journal: J Cell Sci
Title: FRMD4A-cytohesin signaling modulates the cellular release of tau.
Volume: 129
Issue: 10
Pages: 2003-15
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Publication
22323536 | -
First Author: Zhao W
Year: 2012
Journal: J Immunol
Title: E3 ubiquitin ligase tripartite motif 38 negatively regulates TLR-mediated immune responses by proteasomal degradation of TNF receptor-associated factor 6 in macrophages.
Volume: 188
Issue: 6
Pages: 2567-74
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Publication
23056470 | -
First Author: Xue Q
Year: 2012
Journal: PLoS One
Title: TRIM38 negatively regulates TLR3-mediated IFN-β signaling by targeting TRIF for degradation.
Volume: 7
Issue: 10
Pages: e46825
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Publication
24434549 | -
First Author: Hu MM
Year: 2014
Journal: Proc Natl Acad Sci U S A
Title: TRIM38 inhibits TNFα- and IL-1β-triggered NF-κB activation by mediating lysosome-dependent degradation of TAB2/3.
Volume: 111
Issue: 4
Pages: 1509-14
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Publication
21306652 | -
 
First Author: Liu X
Year: 2011
Journal: Virol J
Title: Enterovirus 71 induces degradation of TRIM38, a potential E3 ubiquitin ligase.
Volume: 8
Pages: 61
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Protein Domain
IPR035790 | SPRY/PRY_TRIM38
Type: Domain
Description: This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C terminus of TRIM38, which is also known as RING finger protein 15 (RNF15) or RORET. TRIM proteins are defined by the presence of the tripartite motif RING/B-box/coiled-coil region and are also known as RBCC proteins []. TRIM38 has been shown to act as a suppressor in TOLL-like receptor (TLR)-mediated interferon (IFN)-beta induction by promoting degradation of TRAF6 and NAP1 through the ubiquitin-proteasome system [, ]. Another study has shown that TRIM38 may act as a novel negative regulator for TLR3-mediated IFN-beta signaling by targeting TRIF for degradation []. TRIM38 has been identified as a critical negative regulator in TNFalpha- and IL-1beta-triggered activation of NF-kappaB and MAP Kinases (MAPKs); it causes degradation of two essential cellular components, TGFbeta-associated kinase 1 (TAK1)-associating chaperones 2 and 3 (TAB2/3) []. The degradation is promoted through a lysosomal-dependent pathway, which requires the C-terminal PRY-SPRY of TRIM38. Enterovirus 71 infection induces degradation of TRIM38, suggesting that TRIM38 may play a role in viral infections [].
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Protein Domain
IPR021774 | CUPID
Type: Domain
Description: This entry represents a domain named CUPID (Cytohesin Ubiquitin Protein Inducing Domain) that is found in animal proteins. It is found towards the N-terminal end of Innate immunity activator protein (INAVA, Innate Immune Activator), a risk factor for the chronic inflammatory bowel diseases (IBD). Mice lacking the protein show defects in intestinal barrier integrity at steady state and greater susceptibility to mucosal infection. CUPID is also found towards the N-terminal end of Coiled-coil domain-containing protein 120 (CC120) and C-terminal to the FERM domain in FERM domain-containing protein 4A/B (FRM4A/B), which are implicated in neurite outgrowth, and in human cancer, Alzheimer's, celiac, and heart disease. All appear to bind the ARF-GEF (guanine nucleotide-exchange factors) cytohesin family members, such as proteins (ARF 1-4), which regulate cell membrane and F-actin dynamics. INAVA-CUPID binds cytohesin 2 (also known as ARNO), targets the molecule to lateral membranes of epithelial monolayers, and enables ARNO to affect F-actin assembly that underlies cell-cell junctions and barrier function. In the case of inflammatory signalling, ARNO can coordinate CUPID function by binding and inhibiting CUPID activity of acting as an enhancer of TRAF6 dependent polyubiquitination. In other words, ARNO acts as a negative-regulator of inflammatory responses. In summary, INAVA-CUPID exhibits dual functions, coordinated directly by ARNO, that bridge epithelial barrier function with extracellular signals and inflammation [, , ].
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Protein Coding Gene
MGI:1261423 | Casp8
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:88494 | Creb1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:109298 | Mapkapk2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1915902 | Tab2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:2144023 | Fbxw11
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1346347 | Mapk7
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1346870 | Map2k6
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:104741 | Nfkbia
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1346861 | Mapk8
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913763 | Tab1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1338024 | Mapk11
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1098280 | Crebbp
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:88059 | App
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1342290 | Rps6ka2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:103290 | Rela
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1099800 | Nfkb2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:101835 | Traf2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913839 | Ube2v1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:97312 | Nfkb1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1891456 | Ripk2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1346877 | Map3k7
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:104558 | Rps6ka1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:104752 | Nfkbib
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:107420 | Irak1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913974 | Tab3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:104557 | Rps6ka3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q60778
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
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Protein
P49138
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: false
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Protein
P18654
Organism: Mus musculus/domesticus
Length: 740  
Fragment?: false
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Protein
P45481
Organism: Mus musculus/domesticus
Length: 2441  
Fragment?: false
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Protein
Q9WUI1
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: false
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Protein
Q62073
Organism: Mus musculus/domesticus
Length: 579  
Fragment?: false
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Protein
Q91Y86
Organism: Mus musculus/domesticus
Length: 384  
Fragment?: false
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Protein
Q9WUT3
Organism: Mus musculus/domesticus
Length: 733  
Fragment?: false
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Protein
P18653
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
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Protein
Q62406
Organism: Mus musculus/domesticus
Length: 710  
Fragment?: false
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Protein
Q9Z1E3
Organism: Mus musculus/domesticus
Length: 314  
Fragment?: false
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Protein
Q5SRY7
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: false
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Protein
O89110
Organism: Mus musculus/domesticus
Length: 480  
Fragment?: false
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Protein
Q01147
Organism: Mus musculus/domesticus
Length: 327  
Fragment?: false
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Protein
P70236
Organism: Mus musculus/domesticus
Length: 334  
Fragment?: false
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Protein
Q9WVS8
Organism: Mus musculus/domesticus
Length: 806  
Fragment?: false
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Protein
Q8CF89
Organism: Mus musculus/domesticus
Length: 502  
Fragment?: false
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Protein
P12023
Organism: Mus musculus/domesticus
Length: 770  
Fragment?: false
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Protein
Q9CZY3
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: false
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Protein
P58801
Organism: Mus musculus/domesticus
Length: 539  
Fragment?: false
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Protein
Q04207
Organism: Mus musculus/domesticus
Length: 549  
Fragment?: false
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Protein
P25799
Organism: Mus musculus/domesticus
Length: 971  
Fragment?: false
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Protein
Q9WTK5
Organism: Mus musculus/domesticus
Length: 899  
Fragment?: false
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Publication
10206649 | -
First Author: Park YC
Year: 1999
Journal: Nature
Title: Structural basis for self-association and receptor recognition of human TRAF2.
Volume: 398
Issue: 6727
Pages: 533-8
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Protein
P39428
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
Q3UM74
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
Q4VA12
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Publication
11607847 | -
First Author: Bradley JR
Year: 2001
Journal: Oncogene
Title: Tumor necrosis factor receptor-associated factors (TRAFs).
Volume: 20
Issue: 44
Pages: 6482-91
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Publication
10187771 | J:54313
First Author: Thome M
Year: 1999
Journal: J Biol Chem
Title: Equine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinase.
Volume: 274
Issue: 15
Pages: 9962-8
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Publication
9575168 | J:47675
First Author: Burns K
Year: 1998
Journal: J Biol Chem
Title: MyD88, an adapter protein involved in interleukin-1 signaling.
Volume: 273
Issue: 20
Pages: 12203-9
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Publication
11960013 | J:76299
First Author: Li S
Year: 2002
Journal: Proc Natl Acad Sci U S A
Title: IRAK-4: a novel member of the IRAK family with the properties of an IRAK-kinase.
Volume: 99
Issue: 8
Pages: 5567-72
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Publication
10764746 | J:62785
First Author: Pype S
Year: 2000
Journal: J Biol Chem
Title: TTRAP, a novel protein that associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that inhibits nuclear factor-kappa B activation.
Volume: 275
Issue: 24
Pages: 18586-93
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Publication
12418963 | J:82344
First Author: Yanagisawa K
Year: 2003
Journal: Biochem J
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